Purified Sox-2 Protein
Purified Sox-2 Protein - Related Videos
11:22
GST-His purification: A Two-step Affinity Purification Protocol Yielding Full-length Purified Proteins
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Cited by 18 •
2013
In the present protocol, we demonstrate a highly efficient and cost-effective small-scale protein purification method, which allows purification of recombinant proteins by uniquely combining a cleavable GST-tag and a small His-tag.
09:35
Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Cited by 9 •
2017
Here we present protocols for affinity purification of protein complexes and their separation by blue native PAGE, followed by protein correlation profiling using label free quantitative mass spectrometry. This method is useful to resolve interactomes into distinct protein complexes.
11:21
Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells
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Cited by 5 •
2010
This protocol describes a general approach to perform photoconversion of fluorescent proteins on a confocal laser scanning microscope. We describe procedures for the photoconversion of puried protein samples, as well as for dual-probe optical highlighting in live cells with mOrange2 and Dronpa.
03:54
Nickel Affinity Chromatography-Based Protein Purification: A Technique to Purify Polyhistidine-Tagged Recombinant Proteins from Bacterial Cell Lysate
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2025
In this video, we demonstrate the nickel affinity chromatography technique to purify histidine-tagged pyrophosphokinase enzymes from Clostridium difficile bacteria.
09:59
Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
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Cited by 7 •
2015
Described here is a rapid and effective procedure for functional reconstitution of purified wild-type and mutant CFTR protein that preserves activity for this chloride channel, which is defective in Cystic Fibrosis. Iodide efflux from reconstituted proteoliposomes mediated by CFTR allows studies of channel activity and the effects of small molecules.
FAQs
The HMG domain recognizes particular DNA sequences and bends the DNA helix as part of the binding event. This structural change can alter how nearby regulatory elements are presented to Sox-2 or associated proteins. In biochemical experiments, measuring DNA binding together with DNA bending helps distinguish simple sequence recognition from structural regulation of transcription.
Partner proteins can work with Sox-2 to influence transcriptional regulation, so DNA binding by Sox-2 alone may not reproduce the full regulatory mechanism. Adding defined interaction partners in vitro allows researchers to examine whether they modify Sox-2 activity or support regulatory complex formation. This approach connects protein-protein interactions with control of cell identity and developmental potential.
A defined preparation separates Sox-2 activity from many uncontrolled cellular variables. Researchers can examine DNA binding, protein interactions, or transcriptional regulation under controlled biochemical conditions and relate the observed outcome to a specific component. This control improves reproducibility and helps clarify which molecular interactions contribute to Sox-2 function.
An investigator can expose purified Sox-2 protein to DNA containing a relevant recognition sequence and then evaluate the resulting binding or DNA-structure change. Because the preparation is isolated, the assay can focus on the HMG domain's sequence recognition and helix bending. Such measurements provide a direct molecular test of Sox-2 DNA interaction.
Purified Sox-2 supports controlled in vitro assays that examine DNA binding, protein-protein interactions, and transcriptional regulation. These assay types address complementary questions: whether Sox-2 recognizes DNA, how it associates with partner proteins, and how those molecular events influence regulatory activity. Using the same defined preparation can help connect results across these experimental levels.
Its defined composition supports reproducible structural studies and assay development by reducing uncertainty about the protein component being examined. Researchers can use the preparation to build controlled experiments around Sox-2 interactions with DNA or partner proteins, then relate the resulting molecular observations to pluripotency, stem-cell maintenance, or cellular reprogramming.